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Epidermal growth factor receptor (EGFR), also known as HER1 and ErbB-1, is a cell surface receptor and member of the EGF family of receptor tyrosine kinases with roles in cell proliferation, differentiation, and survival.1,2 It is a transmembrane receptor composed of an intracellular tyrosine kinase domain, a transmembrane lipophilic segment, and an extracellular domain that is expressed in epithelial, mesenchymal, and neuronal tissues.1,2,3 Under unstimulated conditions, EGFR is an auto-inhibited monomer in the plasma membrane.1 Upon canonical ligand binding, EGFR undergoes homodimerization or heterodimerization with HER2, HER3, or HER4, which induces a conformational change in the cytoplasmic domain that facilitates autophosphorylation and intracellular signaling. EGFR contains five C-terminal autophosphorylation sites, namely tyrosine 1068 (Tyr1068), Tyr1148, Tyr1173, Tyr1086, and Tyr992.4 EGFR (phospho-Tyr1068) is associated with prolonged progression-free survival in patients with non-small cell lung cancer (NSCLC). Cayman’s EGFR (Phospho-Tyr1068) Rabbit Monoclonal Antibody can be used for Western blot (WB).
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1. Emerging functions of the EGFR in cancer. Mol. Oncol. 12(1), 3-20 (2018).
2. Review of epidermal growth factor receptor biology. Int. J. Radiat. Oncol. Biol. Phys. 59(2 Suppl), 21-26 (2004).
3. Distribution and function of EGFR in human tissue and the effect of EGFR tyrosine kinase inhibition. Anticancer Res. 23(5A), 3639-3650 (2003).
4. Phosphorylated EGFR expression may predict outcome of EGFR-